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Review
. 2000 Apr;4(2):140-7.
doi: 10.1016/s1367-5931(99)00066-6.

Structure and chemistry of the copper chaperone proteins

A C Rosenzweig  1 , T V O'Halloran
Affiliations
Review

Structure and chemistry of the copper chaperone proteins

A C Rosenzweig et al. Curr Opin Chem Biol. 2000 Apr.

Abstract

Major advances have been made in the past year towards an understanding of the structure and chemistry of copper chaperone proteins. Three-dimensional structures of Atx1, CopZ, yCCS, and hCCSdII were determined, and reveal a remarkable structural similarity between chaperones and target proteins. In addition, biochemical studies of CCS suggested that chaperones are required in vivo because intracellular copper concentrations are extremely low and also indicated that copper transfer occurs via a direct protein-protein interaction.

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